Reviewed,
UniProtKB/Swiss-Prot O05820 (MBTG_MYCTU)
Last modified
February 9, 2010.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: L-lysine 6-monooxygenase mbtG EC=1.14.13.59 Alternative name(s): Lysine 6-N-hydroxylase Lysine N(6)-hydroxylase Lysine-N-oxygenase Mycobactin synthetase protein G | ||||
| Gene names |
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| Organism | Mycobacterium tuberculosis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1773 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 431 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | Flavoprotein monooxygenase required for N-hydroxylation of the two acylated lysine residues during mycobactin assembly, thus producing the hydroxamate groups necessary for iron sequestration. Is also able, but less efficiently, to hydroxylate L-lysine (non acylated) in vitro. Ref.3 Ref.4 |
| Catalytic activity | L-lysine + NADPH + O2 = N(6)-hydroxy-L-lysine + NADP+ + H2O. |
| Cofactor | FAD. Ref.4 |
| Pathway | |
| Induction | Induced by iron starvation conditions and during infection of human THP-1 macrophages. Transcriptionally repressed by ideR and iron By similarity. |
| Sequence similarities | Belongs to the lysine N(6)-hydroxylase/L-ornithine N(5)-oxygenase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Ion transport Iron transport Transport |
| Domain | Signal |
| Ligand | FAD Flavoprotein Iron NADP |
| Molecular function | Monooxygenase Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | iron ion transport Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | L-lysine 6-monooxygenase (NADPH) activity Inferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX842579 Genomic DNA. Translation: CAB08475.1. AE000516 Genomic DNA. Translation: AAK46741.1. |
| PIR | A70588. |
| RefSeq | NP_216894.1. NP_336927.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 885648. 925901. |
| GenomeReviews | Gene locus MT2446 in contig AE000516_GR. |
| KEGG | mtc:MT2446. mtu:Rv2378c. |
| TIGR | MT2446. |
Organism-specific databases | |
| TubercuList | Rv2378c. |
Phylogenomic databases | |
| HOGENOM | HBG432039. |
| OMA | SIAQFWH. |
Enzyme and pathway databases | |
| BRENDA | 1.14.13.59. 809. |
Family and domain databases | |
| ProtoNet | Search... |
Entry information
| Entry name | MBTG_MYCTU | ||||||||
| Accession | Primary (citable) accession number: O05820 Secondary accession number(s): Q7D793 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


